Přehled

Project summary

One of the biggest puzzles in protein evolution is the selection of its amino acid alphabet. Only about half of the canonical alphabet was available prebiotically while the evolutionary “late” amino acids developed through biosynthetic pathways or early life. At the same time, many other alpha-amino acids (that are not part of today’s protein alphabet) were available to use.

This project aims to explore the structure/function-forming potential of the proteinogenic and non-canonical yet prebiotically abundant amino acids (such as aminobutyric and diaminobutyric acid). An algorithm used in our group for design of random sequence protein libraries will be modified to design sequences incorporating unnatural amino acids, using codon reassignment. Commercial and home-made cell-free protein translation systems will be modified in collaboration with our international partners to allow for synthesis of such proteins and protein libraries. Finally, the structural and functional properties of such proteins will be analysed in our group.

The results of this project will provide structural and functional consequences of the most prebiotically abundant non-canonical amino acids and help elucidate the protein structure/function factors in the transitions of protein alphabet evolution.

Profile of an ideal candidate: MSc or equivalent in Chemistry or Biology or a related field, good communication skills in English, background in bioinformatics, molecular biology and biochemistry.